title: Proteomic analysis of human transplanted submandibular gland in patients with epiphora after transplantation.
abstract: Submandibular gland autotransplantation is effective for treating severe dry eye syndrome. However, more than 40% of patients show epiphora within 3-6 months after treatment. The mechanism underlying the hypersecretion in epiphora remains to be elucidated for developing novel interventions. Since salivary gland secretion is dependent on a variety of proteins, we analyzed the changes in protein expression in transplanted glands of epiphora patients with 2-D gel electrophoresis and electrospray ionization quadrupole/time-of-flight mass spectrometry and evaluated their possible roles in epiphora. There were 23 proteins that showed altered expression in the glands of epiphora patients, 15 being up-expressed and 8 being down-expressed. The expression of secretory proteins was decreased in these glands, including alpha-amylase, cystatin S, SA, and SN. In contrast, cytoskeletal proteins were all up-regulated, including actin and vimentin. Immunofluorescence revealed that the intensity ratio of F-actin in apical and lateral cytoplasm to total F-actin in acini was decreased in the glands of epiphora patients. Carbachol stimulation induced a similar redistribution of F-actin in the control glands. Phosphorylation of extracellular signal-regulated kinase 1/2 (ERK1/2) was increased in both carbachol-stimulated and epiphora glands. Preincubation of submandibular glands with ERK1/2 inhibitors PD98059 or U0126 inhibited carbachol-induced F-actin redistribution. These results indicated that differentially expressed proteins participated in the hypersecretion of transplanted submandibular glands and the redistribution of F-actin might be involved in this hypersecretion in an ERK1/2-dependent manner.
authors.affiliation: Center for Salivary Gland Diseases of Peking University School and Hospital of Stomatology, Department of Physiology and Pathophysiology, Peking University Health Science Centre and Key Laboratory of Molecular Cardiovascular Sciences, Ministry of Education, Beijing, China.
authors.forename: Chong
authors.initials: C
authors.lastname: Ding
authors.forename: Yan
authors.initials: Y
authors.lastname: Zhang
authors.forename: Xin
authors.initials: X
authors.lastname: Peng
authors.forename: Yang
authors.initials: Y
authors.lastname: Wang
authors.forename: Lei
authors.initials: L
authors.lastname: Zhang
authors.forename: Xin
authors.initials: X
authors.lastname: Cong
authors.forename: Qian-Wen
authors.initials: QW
authors.lastname: Ding
authors.forename: Ruo-Lan
authors.initials: RL
authors.lastname: Xiang
authors.forename: Li-Ling
authors.initials: LL
authors.lastname: Wu
authors.forename: Guang-Yan
authors.initials: GY
authors.lastname: Yu
mesh_terms: D000199:Actins / Q000378:metabolism; D002070:Butadienes; D002217:Carbachol; D015891:Cystatins / Q000378:metabolism; D005419:Flavonoids; D020869:Gene Expression Profiling; D006801:Humans; D007766:Lacrimal Apparatus Diseases / Q000209:etiology / Q000378:metabolism*; D008856:Microscopy, Fluorescence; D048052:Mitogen-Activated Protein Kinase 3 / Q000378:metabolism; D009570:Nitriles; D016377:Organ Transplantation / Q000009:adverse effects*; D010766:Phosphorylation; D011506:Proteins / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*; D013363:Submandibular Gland / Q000378:metabolism* / Q000637:transplantation*; D014746:Vimentin / Q000378:metabolism; D000516:alpha-Amylases / Q000378:metabolism
chemical_list: D000199:Actins; D002070:Butadienes; D015891:Cystatins; D005419:Flavonoids; D009570:Nitriles; D011506:Proteins; C113580:U 0126; D014746:Vimentin; D002217:Carbachol; D048052:Mitogen-Activated Protein Kinase 3; D000516:alpha-Amylases; C093973:2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one